Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

Scott Bailey, William K. Eliason, Thomas A. Steitz

Research output: Contribution to journalArticle

Abstract

The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.

Original languageEnglish (US)
Pages (from-to)459-463
Number of pages5
JournalScience
Volume318
Issue number5849
DOIs
StatePublished - Oct 19 2007
Externally publishedYes

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DnaB Helicases
DNA Primase
DNA
Static Electricity
Catalytic Domain
Binding Sites

ASJC Scopus subject areas

  • General

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Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. / Bailey, Scott; Eliason, William K.; Steitz, Thomas A.

In: Science, Vol. 318, No. 5849, 19.10.2007, p. 459-463.

Research output: Contribution to journalArticle

Bailey, Scott ; Eliason, William K. ; Steitz, Thomas A. / Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. In: Science. 2007 ; Vol. 318, No. 5849. pp. 459-463.
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